Evidence map›Paper›PMID 31655893›Full record

ArticleEuropean biophysics journal : EBJ2019

Effect of lipid saturation on amyloid-beta peptide partitioning and aggregation in neuronal membranes: molecular dynamics simulations.

Nikolaos Ntarakas, Inna Ermilova, Alexander P Lyubartsev

Open access · hybridAbstract read
In one paragraph

Article in European biophysics journal : EBJ, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.5field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed, 25 citations in OpenAlex.

  1. Decoding Solubility Signatures from Amyloid Monomer Energy Landscapes.Journal of chemical theory and computation · 2025
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Computer simulations of protein-membrane systems.Progress in molecular biology and translational science · 2020
    Article
  10. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Nikolaos NtarakasDepartment of Materials and Environmental Chemistry, Stockholm's University, 10691, Stockholm, Sweden.
Inna ErmilovaDepartment of Materials and Environmental Chemistry, Stockholm's University, 10691, Stockholm, Sweden.
Alexander P LyubartsevDepartment of Materials and Environmental Chemistry, Stockholm's University, 10691, Stockholm, Sweden. alexander.lyubartsev@mmk.su.se.ORCID http://orcid.org/0000-0002-9390-5719
Stockholm University · SE

Funding

Vetenskapsrådet 2017-03950
6 · The paper itself

Abstract

Aggregation of amyloid-[Formula: see text] (Aβ) peptides, cleaved from the amyloid precursor protein, is known as a precursor of the Alzheimer's disease (AD). It is also known that Alzheimer's disease is characterized by a substantial decrease of the amount of polyunsaturated lipids in the neuronal membranes of the frontal gray matter. To get insight into possible interconnection of these phenomena, we have carried out molecular dynamics simulations of two fragments of A[Formula: see text] peptide, A[Formula: see text][Formula: see text] and A[Formula: see text][Formula: see text], in four different lipid bilayers: two monocomponent ones (14:0-14:0 PC, 18:0-22:6 PC), and two bilayers containing mixtures of 18:0-18:0 PE, 22:6-22:6 PE, 16:0-16:0 PC and 18:1-18:1 PC lipids of composition mimicking neuronal membranes in a "healthy" and "AD" brain. The simulations showed that the presence of lipids with highly unsaturated 22:6cis fatty acids chains strongly affects the interaction of amyloid-[Formula: see text] peptides with lipid membranes. The polyunsaturated lipids cause stronger adsorption of A[Formula: see text]-peptides by the membrane and lead to weaker binding between peptides when the latter form aggregates. This difference in the behaviour observed in monocomponent bilayers is propagated in a similar fashion to the mixed membranes mimicking composition of neuronal membranes in "healthy" and "AD" brains, with "healthy" membrane having higher fraction of polyunsaturated lipids. Our simulations give strong indication that it can be physical-chemical background of the interconnection between amyloid fibrillization causing Alzheimer's disease, and content of polyunsaturated lipids in the neuronal membranes.

Indexed as

Molecular Dynamics SimulationProtein AggregatesAmyloid beta-PeptidesCell MembraneLipid BilayersMembrane LipidsNeuronsAmyloid beta-PeptidesLipid BilayersMembrane LipidsProtein AggregatesAlzheimer diseaseAmyloid-beta peptidesLipid bilayersMolecular dynamicsOmega-3PhospholipidsPolyunsaturated fatty acids

Identifiers

PMID31655893
PMCPMC6853862
OpenAlexW2981983807

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.